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Production, purification, crystallization and preliminary X-ray analysis of adeno-associated virus serotype 8
- Source :
- Acta crystallographica. Section F, Structural biology and crystallization communications. 61(Pt 6)
- Publication Year :
- 2005
-
Abstract
- Adeno-associated viruses (AAVs) are actively being developed for clinical gene-therapy applications and the efficiencies of the vectors could be significantly improved by a detailed understanding of their viral capsid structures and the structural determinants of their tissue-transduction interactions. AAV8 is approximately 80% identical to the more widely studied AAV2, but its liver-transduction efficiency is significantly greater than that of AAV2 and other serotypes. The production, purification, crystallization and preliminary X-ray crystallographic analysis of AAV8 viral capsids are reported. The crystals diffract X-rays to 3.0 A resolution using synchrotron radiation and belong to the hexagonal space group P6(3)22, with unit-cell parameters a = 257.5, c = 443.5 A. The unit cell contains two viral particles, with ten capsid viral protein monomers per crystallographic asymmetric unit.
- Subjects :
- Insecta
Viral protein
viruses
Biophysics
Biology
medicine.disease_cause
Biochemistry
law.invention
Cell Line
Viral Proteins
Capsid
X-Ray Diffraction
Structural Biology
law
Genetics
medicine
Animals
Crystallization
Cloning, Molecular
Adeno-associated virus
Parvovirus
Resolution (electron density)
Space group
Dependovirus
Condensed Matter Physics
biology.organism_classification
Crystallography
Crystallization Communications
X-ray crystallography
Capsid Proteins
Subjects
Details
- ISSN :
- 17443091
- Volume :
- 61
- Issue :
- Pt 6
- Database :
- OpenAIRE
- Journal :
- Acta crystallographica. Section F, Structural biology and crystallization communications
- Accession number :
- edsair.doi.dedup.....845d6d710f997ea146b07f91e92c3917